Characterization of MiFUT11 from Mangifera indica L.: A functional core α1,3-fucosyltransferase potentially involved in the biosynthesis of immunogenic carbohydrates in mango fruit
2019
Abstract In higher plants, asparagine-linked
oligosaccharides(N-
glycans) in glycoproteins carry unique carbohydrate epitopes, namely, a core α1,3-
fucoseand/or a β1,2-xylose, which are common determinants responsible for the
cross-reactivityof plant glycoproteins due to their strong immunogenicity. While these determinants and the relevant genes have been well characterized for
herbaceous plants, information concerning whether many food plants cross-react with airborne pollens is not available. In this paper, we report on the characterization of a novel core α1,3-
fucosyltransferasegene identified from
Mangiferaindica L., one of the major plants potentially related to
food allergy. Based on sequence information of plant homologues, we amplified a candidate cDNA (MiFUT11) from pericarp tissue. An in vitro assay demonstrated that the recombinant MiFUT11 protein transfers a
fucoseunit onto both non-
fucosylatedand core α1,6-
fucosylated
oligosaccharides. A glycoform analysis using MALDI-TOF mass spectrometry showed that the introduction of the MiFUT11 cDNA increased the production of a core α1,3- and α1,6-
fucosylatedpauci-mannosidic
oligosaccharidein
SpodopteraSf21 cells. Our findings suggest that MiFUT11 is a functional core α1,3-
fucosyltransferasegene that is involved in the assembly of
cross-reactiveN-
glycansin mango fruit.
Keywords:
-
Correction
-
Source
-
Cite
-
Save
51
References
0
Citations
NaN
KQI